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BM23_DROME
ID   BM23_DROME              Reviewed;         117 AA.
AC   Q9V8F5; Q8SY64;
DT   02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 2.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Bomanin Bicipital 1 {ECO:0000312|FlyBase:FBgn0034328};
DE   AltName: Full=Bomanin-23 {ECO:0000303|PubMed:25915418};
DE   AltName: Full=Immune-induced peptide 23 {ECO:0000312|FlyBase:FBgn0034328};
DE            Short=DIM-23 {ECO:0000312|FlyBase:FBgn0034328};
DE            Short=DIM23 {ECO:0000303|PubMed:9736738};
DE   Flags: Precursor;
GN   Name=BomBc1 {ECO:0000312|FlyBase:FBgn0034328};
GN   Synonyms=Bom23 {ECO:0000312|FlyBase:FBgn0034328},
GN   IM23 {ECO:0000312|FlyBase:FBgn0034328};
GN   ORFNames=CG15066 {ECO:0000312|FlyBase:FBgn0034328};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227 {ECO:0000312|EMBL:AAF57712.2};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2] {ECO:0000305}
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC   TISSUE=Head {ECO:0000269|PubMed:12537569};
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [4] {ECO:0000305}
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY BACTERIA, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=Oregon-R {ECO:0000303|PubMed:9736738};
RC   TISSUE=Hemolymph {ECO:0000303|PubMed:9736738};
RX   PubMed=9736738; DOI=10.1073/pnas.95.19.11342;
RA   Uttenweiler-Joseph S., Moniatte M., Lagueux M., van Dorsselaer A.,
RA   Hoffmann J.A., Bulet P.;
RT   "Differential display of peptides induced during the immune response of
RT   Drosophila: a matrix-assisted laser desorption ionization time-of-flight
RT   mass spectrometry study.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:11342-11347(1998).
RN   [5] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 21-117, DISULFIDE BONDS, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=Oregon-R {ECO:0000303|Ref.5}; TISSUE=Hemolymph {ECO:0000303|Ref.5};
RA   Bulet P., Charlet M., Ehret-Sabatier L.;
RL   Submitted (JUL-2002) to UniProtKB.
RN   [6]
RP   FUNCTION.
RX   PubMed=25915418; DOI=10.1371/journal.ppat.1004876;
RA   Clemmons A.W., Lindsay S.A., Wasserman S.A.;
RT   "An effector Peptide family required for Drosophila toll-mediated
RT   immunity.";
RL   PLoS Pathog. 11:E1004876-E1004876(2015).
RN   [7]
RP   FUNCTION.
RX   PubMed=29920489; DOI=10.1159/000489831;
RA   Lindsay S.A., Lin S.J.H., Wasserman S.A.;
RT   "Short-Form Bomanins Mediate Humoral Immunity in Drosophila.";
RL   J. Innate Immun. 10:306-314(2018).
CC   -!- FUNCTION: Secreted immune-induced peptide induced by Toll signaling
CC       (PubMed:9736738). Has a role in resistance to bacterial and fungal
CC       infections (PubMed:25915418, PubMed:29920489).
CC       {ECO:0000269|PubMed:25915418, ECO:0000269|PubMed:29920489,
CC       ECO:0000269|PubMed:9736738}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29920489,
CC       ECO:0000269|PubMed:9736738, ECO:0000269|Ref.5}.
CC   -!- TISSUE SPECIFICITY: Hemolymph (at protein level).
CC       {ECO:0000269|PubMed:29920489, ECO:0000269|PubMed:9736738,
CC       ECO:0000269|Ref.5}.
CC   -!- INDUCTION: By bacterial infection (at protein level) (PubMed:9736738).
CC       Detected within 24 hours of infection (at protein level)
CC       (PubMed:9736738). {ECO:0000269|PubMed:9736738}.
CC   -!- MASS SPECTROMETRY: Mass=9482.41; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:9736738};
CC   -!- MISCELLANEOUS: Not induced after bacterial challenge in strains
CC       carrying a loss-of-function mutation for Toll. Constitutively expressed
CC       in Toll gain-of-function mutants. {ECO:0000269|PubMed:9736738}.
CC   -!- SIMILARITY: Belongs to the bomanin family. {ECO:0000305}.
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DR   EMBL; AE013599; AAF57712.2; -; Genomic_DNA.
DR   EMBL; AY071762; AAL49384.1; -; mRNA.
DR   RefSeq; NP_611318.2; NM_137474.5.
DR   AlphaFoldDB; Q9V8F5; -.
DR   IntAct; Q9V8F5; 8.
DR   STRING; 7227.FBpp0085908; -.
DR   PaxDb; Q9V8F5; -.
DR   DNASU; 37099; -.
DR   EnsemblMetazoa; FBtr0086729; FBpp0085908; FBgn0034328.
DR   GeneID; 37099; -.
DR   KEGG; dme:Dmel_CG15066; -.
DR   CTD; 37099; -.
DR   FlyBase; FBgn0034328; BomBc1.
DR   VEuPathDB; VectorBase:FBgn0034328; -.
DR   HOGENOM; CLU_2294530_0_0_1; -.
DR   InParanoid; Q9V8F5; -.
DR   OMA; NSPDAYP; -.
DR   OrthoDB; 1553482at2759; -.
DR   PhylomeDB; Q9V8F5; -.
DR   BioGRID-ORCS; 37099; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 37099; -.
DR   PRO; PR:Q9V8F5; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0034328; Expressed in capitellum (Drosophila) and 13 other tissues.
DR   ExpressionAtlas; Q9V8F5; baseline and differential.
DR   Genevisible; Q9V8F5; DM.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0019731; P:antibacterial humoral response; IDA:UniProtKB.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IEP:FlyBase.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0009617; P:response to bacterium; HEP:FlyBase.
DR   InterPro; IPR013172; Bomanin.
DR   Pfam; PF08194; DIM; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Immunity; Innate immunity;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..117
FT                   /note="Bomanin Bicipital 1"
FT                   /id="PRO_0000021508"
FT   DISULFID        29..32
FT                   /evidence="ECO:0000269|Ref.5"
FT   DISULFID        107..110
FT                   /evidence="ECO:0000269|Ref.5"
FT   CONFLICT        66
FT                   /note="L -> P (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        86..87
FT                   /note="AQ -> TR (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   117 AA;  11552 MW;  DFFCF1230AFD6FF7 CRC64;
     MKCLILSFAI FVVLASQATA GNVIIGGVCQ DCSPPVAENV VVGGQSYRTG RPGQGTVYIN
     SPGAYLGALD GPIRRTGAGG GGGGGAQYPD GYSGRLPGGT YLHNKDCVGC SISGGGD
 
 
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